Tmem33 antibody - middle region (ARP47398_P050)
- Known as:
- Tmem33 (anti-) - middle region (ARP47398_P050)
- Catalog number:
- arp47398_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- Tmem33 antibody - middle region (ARP47398_P050)
Related genes to: Tmem33 antibody - middle region (ARP47398_P050)
- Gene:
- TMEM33 NIH gene
- Name:
- transmembrane protein 33
- Previous symbol:
- -
- Synonyms:
- FLJ10525, Pom33
- Chromosome:
- 4p13
- Locus Type:
- gene with protein product
- Date approved:
- 2004-07-28
- Date modifiied:
- 2019-03-07
Related products to: Tmem33 antibody - middle region (ARP47398_P050)
Related articles to: Tmem33 antibody - middle region (ARP47398_P050)
- Lung adenocarcinoma is a common type of lung cancer with high incidence and mortality rates. TMEM33, a tumor-associated protein, has not been fully elucidated in lung adenocarcinoma. To explore the expression of TMEM33 in lung adenocarcinoma, its impact on tumor progression, and its role in the PI3K/AKT/mTOR signaling pathway. Key genes associated with lung adenocarcinoma were screened using the Gene Expression Omnibus (GEO) dataset GSE140797 in combination with a weighted correlation network analysis (WGCNA). Gene Ontology (GO) functional enrichment and Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway analyses were performed on these key genes. TMEM33 expression in Lung adenocarcinoma patients was validated using data from the TCGA database. The directly interactive molecules were screened through a bioinformatics method. Cellular assays (Western Blot, CCK8, colony formation, scratch assay, Trans well assay) and a nude mouse model were used to investigate the effects of TMEM33 on cell proliferation, migration, and tumor growth. TMEM33 is highly expressed in lung adenocarcinoma tissues (P < 0.05) and associated with poor prognosis. Overexpression of TMEM33 promotes cell proliferation and migration, and activates the PI3K/AKT/mTOR signaling pathway (P < 0.01). In the nude mouse model, TMEM33 overexpression increases tumor volume (P < 0.001), and PI3K/AKT pathway inhibition suppresses these effects (P < 0.05, P < 0.01). TMEM33 acts as an oncogene in lung adenocarcinoma by activating the PI3K/AKT/mTOR pathway, providing new therapeutic targets. - Source: PubMed
Publication date: 2026/06/24
Wudu MuliLou HaijunMa YuyuZhang ZhenyuAlimujiang SureyanDeng YanchaoJing XiaoliangMeng MenggenXu ZhipengHasim Ayshamgul - Diabetic erectile dysfunction (DMED) is a common complication among male patients with diabetes. Therapies primarily based on phosphodiesterase type 5 inhibitors (PDE5Is) often yield suboptimal results. Extracellular vesicles (EVs) have emerged as a promising therapeutic strategy; however, their clinical translation is hindered by rapid in vivo clearance and limited inherent bioactivity. Therefore, we developed an innovative combined therapeutic approach. First, we fabricated an injectable, thermosensitive hydrogel (ECMTA-Hydrogel) by combining a decellularized porcine corpus cavernosum extracellular matrix (ECM) with tannic acid, which exhibits excellent biocompatibility and rapid gelation at body temperature (37 °C), enabling prolonged local retention of EVs within the corpus cavernosum. Second, we pretreated mesenchymal stem cells (MSCs) with pioglitazone to generate engineered EVs (PGZ-EVs) with enhanced bioactivity. Experiments confirmed that the ECMTA-Hydrogel facilitates sustained release of PGZ-EVs, extending their duration of action. In a DMED rat model, the combined ECMTA-PGZ-EVs therapy demonstrated superior efficacy, markedly improving erectile function and effectively reversing pathological phenotypic switching and apoptosis in corpus cavernosum smooth muscle cells (CCSMCs). Mechanistically, we identified that miR-203a-3p, highly enriched in PGZ-EVs, directly targets and suppresses the endoplasmic reticulum transmembrane protein TMEM33, thereby mitigating diabetes-induced endoplasmic reticulum stress (ERS). This pathway represents the key mechanism underlying the cytoprotective effects of PGZ-EVs. In summary, this study not only establishes an efficient natural matrix hydrogel-based delivery system but also augments the therapeutic potential of EVs via engineered modification. Furthermore, we elucidate a novel mechanism involving the miR-203a-3p/TMEM33/ERS axis, offering a promising therapeutic strategy for the clinical management of DMED. - Source: PubMed
Publication date: 2026/04/14
Liu HaoZang ZhenjieZhao DanfengZhang JingWang ZhenqingFu QiangZhang Keqin - - Source: PubMed
Publication date: 2026/01/29
Li YingYu HuifangWang JianjianKang Kai - Improving responses to cancer immunotherapies requires deeper insight into the cellular mechanisms governing T cell-mediated anti-tumor immunity. TMEM33 is an endoplasmic reticulum-resident transmembrane protein enriched across multiple tumor types, with reported functions in anti-viral immunity as well as calcium and lipid homeostasis, yet its role in tumor immunosurveillance remains unknown. Using murine genetic models, we demonstrate that host TMEM33 constrains anti-tumor CD8 T cell responses. Constitutive mice exhibited delayed melanoma tumor growth and increased CD8 T cell infiltration. Antigen-specific CD8 compartments in tumors of mice showed TCF-1PD-1 progenitor-exhausted cell (Tpex) enrichment, elevated effector function and reduced exhaustion, alongside improved effector memory expansion and T-bet expression in draining lymph nodes. We highlight that TMEM33 functions intrinsically within the T cell compartment, as TMEM33 deletion (1) enhanced polyclonal activation of naive CD8 T cells , (2) promoted preferential Tpex accumulation among adoptively transferred naive OT-I cells in B16F10-OVA tumors and draining lymph nodes, and (3) improved the potency of -expanded OT-I cells in controlling tumor growth during adoptive cell therapy. Finally, in a large, prospectively recruited metastatic melanoma cohort, lower expression in patient CD8 T cells significantly correlated with improved survival and elevated (encoding TCF-1). Collectively, our findings define TMEM33 as a formerly unrecognized intrinsic determinant of tumor-directed CD8 T cell fate that limits Tpex maintenance, and restrains cell therapy responses, suggesting that its modulation may strengthen immunotherapeutic efficacy. - Source: PubMed
Publication date: 2026/01/02
Jackson Matthew TZhao TianmingMilotay GusztavPedroza-Pacheco IsabelaCai YanshuWillis ClairePhyu Su MBeernaert BrunoKwon Jamie TwEstephan HalaAlmeida Vinnycius PereiraAggelakopoulou MariaPanetti SilviaZierhut ChristianElliott TimAdamopoulou EleniRehwinkel JanSim Malcolm JwGrover AmitGabrilovich Dmitry IFairfax Benjamin PHonoré EricWithers David RChristianson John CParkes Eileen E - Rafeesome, a newly identified multivesicular body (MVB)-like organelle, forms through the fusion of RAB22A-mediated ER-derived noncanonical autophagosomes with RAB22A-positive early endosomes. However, the mechanism underlying the formation of RAB22A-mediated noncanonical autophagosomes remains unclear. Herein, we report a secretory ER-phagy pathway in which the assembly of RAB22A/TMEM33/RTN4 induces the clustering of high-molecular-weight RTN4 oligomers, leading to ER membrane remodeling. This remodeling drives the biogenesis of ER-derived RTN4-positive noncanonical autophagosomes, which are ultimately secreted as TMEM33-marked RAB22A-induced extracellular vesicles (R-EVs) via Rafeesome. Specifically, RAB22A interacts with the tubular ER membrane protein TMEM33, which binds to the TM2 domain of the ER-shaping protein RTN4, promoting RTN4 homo-oligomerization and thereby generating RTN4-enriched microdomains. Consequently, the RTN4 microdomains may induce high curvature of the ER, facilitating the bud scission of RTN4-positive vesicles. These vesicles are transported by ATG9A and develop into isolation membranes (IMs), which are then anchored by LC3-II, a process catalyzed by the ATG12-ATG5-ATG16L1 complex, allowing them to grow into sealed RTN4 noncanonical autophagosome. While being packaged into these ER-derived intermediate compartments, ER cargoes bypass lysosomal degradation and are directed to secretory autophagy via the Rafeesome-R-EV route. Our findings reveal a secretory ER-phagy pathway initiated by the assembly of RAB22A/TMEM33/RTN4, providing new insights into the connection between ER-phagy and extracellular vesicles. - Source: PubMed
Publication date: 2025/04/29
Zheng XuepingFang DongmeiShan HaoXiao BeibeiWei DenghuiOuyang YingyiHuo LanqingZhang ZhonghanWu YuanzhongZhang RuhuaKang TiebangGao Ying